ID F5YJ10_TREPZ Unreviewed; 386 AA.
AC F5YJ10;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Aldo/keto reductase {ECO:0000313|EMBL:AEF85639.1};
GN OrderedLocusNames=TREPR_3460 {ECO:0000313|EMBL:AEF85639.1};
OS Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF85639.1, ECO:0000313|Proteomes:UP000009223};
RN [1] {ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RA Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X., Lucey K.,
RA Ballor N.R., Ottesen E., Rosenthal R., Allen A., Leadbetter J.R.,
RA Paulsen I.T.;
RT "Complete sequence of Treponema primitia strain ZAS-2.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEF85639.1, ECO:0000313|Proteomes:UP000009223}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC {ECO:0000313|Proteomes:UP000009223};
RX PubMed=21326336; DOI=10.1038/ismej.2011.3;
RA Rosenthal A.Z., Matson E.G., Eldar A., Leadbetter J.R.;
RT "RNA-seq reveals cooperative metabolic interactions between two termite-gut
RT spirochete species in co-culture.";
RL ISME J. 5:1133-1142(2011).
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DR EMBL; CP001843; AEF85639.1; -; Genomic_DNA.
DR RefSeq; WP_015706831.1; NC_015578.1.
DR AlphaFoldDB; F5YJ10; -.
DR STRING; 545694.TREPR_3460; -.
DR KEGG; tpi:TREPR_3460; -.
DR eggNOG; COG1453; Bacteria.
DR HOGENOM; CLU_023205_3_2_12; -.
DR OrthoDB; 9773828at2; -.
DR Proteomes; UP000009223; Chromosome.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd19096; AKR_Fe-S_oxidoreductase; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR020471; AKR.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43312; D-THREO-ALDOSE 1-DEHYDROGENASE; 1.
DR PANTHER; PTHR43312:SF2; OXIDOREDUCTASE-RELATED; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR PRINTS; PR00069; ALDKETRDTASE.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000009223}.
FT DOMAIN 333..362
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 386 AA; 43345 MW; CDE80BA0250B5F93 CRC64;
MQYREDKVSG NKLSILGLGC MRFSRNMAET ERMILAAIDG GVNYFDTAYI YPNSEETLGT
ILGKHKKRTS VFIATKLPLI VCKGPDDFDK FFNKELERLQ TDYIDYYLMH MITDSAQWEQ
FREWGIEQWI AEKKRAGKIR QAGFSFHGSS VEFLKILNAY PWDFCQIQYN YSNENYQAGK
EGLKAAAAKG IPVMIMEPLL GGKLAAGLPK EAAALFSKTD PTLSPAAWGF RWLWNQSEVS
CVLSGMNTTA QMEDNLRSAE NARPLTDAEL AVYTEVIGLF NRAYKIHCTG CNYCMPCPKG
INIPGCFAAY NASFAQNFTI GMQQFLTSTA AVSKKPHSPR LCVECGKCES HCPQHLPIRK
ALKQVARRME PLPVRLGLSI ARQFLG
//
